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Q5J6J3

- DPP4_TRIRU

UniProt

Q5J6J3 - DPP4_TRIRU

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Protein

Dipeptidyl peptidase 4

Gene
DPP4
Organism
Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Extracellular dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. Contributes to pathogenicity.1 Publication

Catalytic activityi

Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.

pH dependencei

Optimum pH is 7.0-9.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei613 – 6131Charge relay system By similarity
Active sitei690 – 6901Charge relay system By similarity
Active sitei725 – 7251Charge relay system By similarity

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB-KW
  2. serine-type endopeptidase activity Source: InterPro

GO - Biological processi

  1. pathogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease, Serine protease

Keywords - Biological processi

Virulence

Protein family/group databases

MEROPSiS09.008.

Names & Taxonomyi

Protein namesi
Recommended name:
Dipeptidyl peptidase 4 (EC:3.4.14.5)
Alternative name(s):
Dipeptidyl peptidase IV
Short name:
DPP IV
Short name:
DppIV
Gene namesi
Name:DPP4
OrganismiTrichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum)
Taxonomic identifieri5551 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesArthrodermataceaemitosporic ArthrodermataceaeTrichophyton

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
  2. membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515 Reviewed predictionAdd
BLAST
Chaini16 – 775760Dipeptidyl peptidase 4PRO_0000384089Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi81 – 811N-linked (GlcNAc...) Reviewed prediction
Glycosylationi111 – 1111N-linked (GlcNAc...) Reviewed prediction
Glycosylationi154 – 1541N-linked (GlcNAc...) Reviewed prediction
Glycosylationi219 – 2191N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ5J6J3.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S9B family.

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.140.10.30. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002471. Pept_S9_AS.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B.
[Graphical view]
PfamiPF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00131. CARBOXYPEPT_SER_SER. 1 hit.
PS00708. PRO_ENDOPEP_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5J6J3-1 [UniParc]FASTAAdd to Basket

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MKLLSLLMLA GIAQAIVPPR EPRSPTGGGN KLLTYKECVP RATISPRSTS    50
LAWINSEEDG RYISQSDDGA LILQNIVTNT NKTLVAADKV PKGYYDYWFK 100
PDLSAVLWAT NYTKQYRHSY FANYFILDIK KGSLTPLAQD QAGDIQYAQW 150
SPMNNSIAYV RXNDLYIWNN GKTKRITENG GPDIFNGVPD WVYEEEIFGD 200
RFALWFSPDG EYLAYLRFNE TGVPTYTIPY YKNKQKIAPA YPRELEIRYP 250
KVSAKNPTVQ FHLLNIASSQ ETTIPVTAFP ENDLVIGEVA WLSSGHDSVA 300
YRAFNRVQDR EKIVSVKVES KESKVIRERD GTDGWIDNLL SMSYIGNVNG 350
KEYYVDISDA SGWAHIYLYP VDGGKEIALT KGEWEVVAIL KVDTKKKLIY 400
FTSTKYHSTT RHVYSVSYDT KVMTPLVNDK EAAYYTASFS AKGGYYILSY 450
QGPNVPYQEL YSTKDSKKPL KTITSNDALL EKLKEYKLPK VSFFEIKLPS 500
GETLNVKQRL PPNFNPHKKY PVLFTPYGGP GAQEVSQAWN SLDFKSYITS 550
DPELEYVTWT VDNRGTGYKG RKFRSAVAKR LGFLEAQDQV FAAKEVLKNR 600
WADKDHIGIW GXSYGGFLTA KTLETDSGVF TFGISTAPVS DFRLYDSMYT 650
ERYMKTVELN ADGYSETAVH KVDGFKNLKG HYLIQHGTGD DNVHFQNAAV 700
LSNTLMNGGV TADKLTTQWF TDSDHGIRYD MDSTYQYKQL SKMVYDQKQR 750
RPESPPMHQW SKRVLAALFG ERAEE 775
Length:775
Mass (Da):88,021
Last modified:February 15, 2005 - v1
Checksum:i157774F128C6BFDB
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY497021 Genomic DNA. Translation: AAS76665.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY497021 Genomic DNA. Translation: AAS76665.1 .

3D structure databases

ProteinModelPortali Q5J6J3.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi S09.008.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.140.10.30. 1 hit.
3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR002471. Pept_S9_AS.
IPR001375. Peptidase_S9.
IPR002469. Peptidase_S9B.
[Graphical view ]
Pfami PF00930. DPPIV_N. 1 hit.
PF00326. Peptidase_S9. 1 hit.
[Graphical view ]
SUPFAMi SSF53474. SSF53474. 1 hit.
PROSITEi PS00131. CARBOXYPEPT_SER_SER. 1 hit.
PS00708. PRO_ENDOPEP_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Aminopeptidases and dipeptidyl-peptidases secreted by the dermatophyte Trichophyton rubrum."
    Monod M., Lechenne B., Jousson O., Grand D., Zaugg C., Stoecklin R., Grouzmann E.
    Microbiology 151:145-155(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiDPP4_TRIRU
AccessioniPrimary (citable) accession number: Q5J6J3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: February 15, 2005
Last modified: June 11, 2014
This is version 37 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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